Recombinant Heme Oxygenase 1 Monoclonal Antibody (AN301794L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, MCF-7, HepG2, NIH/3T3, BRL, Mouse kidney Verified Samples in IHC: Human spleen, Mouse liver, Rat liver Verified Samples in IF: HeLa, MCF7 Verified Samples in FCM: HeLa, MCF-7 Verified Samples in IP: HeLa cells extracts |
| Dilution | WB 1:2000-1:20000, IHC 1:1000-1:2000, IF 1:50, FCM 1:50-1:100, IP 1:25-1:100 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB, IHC, IF, FCM, IP |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Heme Oxygenase 1 fragment |
| Abbre | Heme Oxygenase 1 |
| Synonyms | HSP, heme oxygenase, heme oxygenase (decycling), bK286B, HO-1 HMOX, HMOX1, HMOX1D, HO-1, HSP32, bK286B10, 32 kD, D8Wsu38e, heat shock protein 32 kD, heat shock protein 32kD, Hemox, Hmox, HMOX 1, HO 1, HO-1 HMOX1, heme oxygenase (decycling) 1, heme oxygenase 1, heat shock protein, 32-kD, HO, HO1, bK286B10, heme oxygenase 1, HMOX1D, HO-1, HSP32 |
| Swissprot | |
| Calculated MW | 32 kDa |
| Observed MW |
32 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Endoplasmic reticulum |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Neuroscience, Cardiovascular, Signal Transduction, Epigenetics and Nuclear Signaling, Cancer, Metabolism |
| Clone No. | A506 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Heme oxygenase 1 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. |
Other Clones
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Unconjugated
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